EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.2.20 | L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe | Streptomyces noursei | the enzyme uses more efficiently Phe-tRNAPhe than any of the Leu-tRNALeu. The efficiency of cyclo(L-phenylalanyl-L-phenylalanyl) synthesis is not affected by the presence of Leu-tRNALeuGAG or Leu-tRNALeuTAA indicating that these molecules do not compete with Phe-tRNAPhe for binding to the enzyme. In contrast, Leu-tRNALeuCAA, Leu-tRNALeuTAG or or Leu-tRNALeuCAG isoacceptors inhibit cyclo(L-phenylalanyl-L-phenylalanyl) synthesis revealing a competition with Phe-tRNAPhe | tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl) | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.2.20 | Streptomyces noursei | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.2.20 | L-leucyl-tRNALeu + L-phenylalanyl-tRNAPhe | the enzyme uses more efficiently Phe-tRNAPhe than any of the Leu-tRNALeu. The efficiency of cyclo(L-phenylalanyl-L-phenylalanyl) synthesis is not affected by the presence of Leu-tRNALeuGAG or Leu-tRNALeuTAA indicating that these molecules do not compete with Phe-tRNAPhe for binding to the enzyme. In contrast, Leu-tRNALeuCAA, Leu-tRNALeuTAG or or Leu-tRNALeuCAG isoacceptors inhibit cyclo(L-phenylalanyl-L-phenylalanyl) synthesis revealing a competition with Phe-tRNAPhe | Streptomyces noursei | tRNALeu + tRNAPhe + cyclo(L-leucyl-L-phenylalanyl) | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.2.20 | AlbC | - |
Streptomyces noursei |
2.3.2.20 | CDPS | - |
Streptomyces noursei |
2.3.2.20 | cyclodipeptide synthase | - |
Streptomyces noursei |